Recombinant Human PSMA4 Protein

Name: Recombinant Human PSMA4 Protein
Brand: Beta LifeScience
SKU: BL-1638PS
Availability: InStock

Collections: Car-nk targets proteins, Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Synonym	Proteasome subunit alpha type-4, Macropain subunit C9, Multicatalytic endopeptidase complex subunit C9, Proteasome component C9, Proteasome subunit L, PSMA4, HC9, PSC9, HsT17706.
Background	Proteasome subunit alpha type 4 (PSMA4) belongs to the peptidase T1A family, which is a 20S core alpha subunit. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. The core structure is comprised of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. PSMA4 is dispersed throughout eukaryotic cells at a high concentration and cleaves peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.
Description	PSMA4 Human Recombinant expressed in E.coli is a single, non-glycosylated polypeptide chain containing 285a.a. (1-261) and having a molecular weight of 32kDa.PSMA4 is fused to a 24a.a. His-tag at N-terminus and purified by unique purification methods.
Source	E.coli
AA Sequence	MGSSHHHHHH SSGLVPRGSH MGSHMSRRYD SRTTIFSPEG RLYQVEYAME AIGHAGTCLG ILANDGVLLA AERRNIHKLL DEVFFSEKIY KLNEDMACSV AGITSDANVL TNELRLIAQR YLLQYQEPIP CEQLVTALCD IKQAYTQFGG KRPFGVSLLY IGWDKHYGFQ LYQSDPSGNY GGWKATCIGN NSAAAVSMLK QDYKEGEMTL KSALALAIKV LNKTMDVSKL SAEKVEIATL TRENGKTVIR VLKQKEVEQL IKKHEEEEAK AEREKKEKEQ KEKDK.
Purity	>95% as determined by SDS-PAGE.
Endotoxin	<1.0 EU per μg by the LAL method.
Formulation	The PSMA4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT and 0.1mM PMSF.
Stability	Recombinant protein is stable for 12 months at -70°C
Usage	For Research Use Only
Storage	Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.